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Biochemical and Immunological Characterization of the DNA Binding Protein (RBP-J Kappa) to Mouse J Kappa Recombination Signal Sequence

Biochemical and Immunological Characterization of the DNA Binding Protein (RBP-J Kappa) to Mouse J Kappa Recombination Signal Sequence

Y Hamaguchi, Y Yamamoto, H Iwanari, S Maruyama, T Furukawa, N Matsunami, T Honjo

J Biochem. 1992 Sep;112(3):314-20.

PMID: 1429518

Abstract:

We have investigated whether J kappa recombination signal sequence (RS) binding protein (RBP-J kappa) has any partial catalytic activities involved in the VDJ recombination reaction, such as cleavage, ligation, and bending of DNA. Murine RBP-J kappa protein purified by J kappa-RS affinity chromatography did not show DNA cleavage activities but contained a strong DNA ligase activity. To obtain a large amount of purified RBP-J kappa protein, recombinant RBP-J kappa was synthesized in Escherichia coli as a fusion protein and also in silkworm cells. Although recombinant RBP-J kappa produced in silkworm cells could bind J kappa-RS, it failed to show either ligase or DNA bending activity. Since the DNA affinity-purified RBP-J kappa has the ligase activity, the RBP-J kappa protein may form a complex with a ligase in vivo. We have raised monoclonal antibodies against the RBP-J kappa fusion protein which was synthesized in E. coli and unable to bind J kappa-RS. Using the anti-RBP-J kappa monoclonal antibody we have shown that the RBP-J kappa protein is expressed ubiquitously in mammalian tissues. The ubiquitous expression of the RBP-J kappa protein is consistent with the hypothesis that the RBP-J kappa protein may have dual function [Furukawa et al. (1991) J. Biol. Chem. 266, 23334-23340].

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4248964	Monoclonal Anti-DNA Ligase I antibody produced in mouse			Price

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